6nch
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of CDP-Chase: Raster data collection== | |
+ | <StructureSection load='6nch' size='340' side='right'caption='[[6nch]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6nch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NCH FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RB5:D-RIBOSE'>RB5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6nch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nch OCA], [https://pdbe.org/6nch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nch RCSB], [https://www.ebi.ac.uk/pdbsum/6nch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nch ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q81EE8_BACCR Q81EE8_BACCR] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Advances in synchrotron technology are changing the landscape of macromolecular crystallography. The two recently opened beamlines at NSLS-II-AMX and FMX-deliver high-flux microfocus beams that open new possibilities for crystallographic data collection. They are equipped with state-of-the-art experimental stations and automation to allow data collection on previously intractable crystals. Optimized data collection strategies allow users to tailor crystal positioning to optimally distribute the X-ray dose over its volume. Vector data collection allows the user to define a linear trajectory along a well diffracting volume of the crystal and perform rotational data collection while moving along the vector. This is particularly well suited to long, thin crystals. We describe vector data collection of three proteins-Akt1, PI3Kalpha, and CDP-Chase-to demonstrate its application and utility. For smaller crystals, we describe two methods for multicrystal data collection in a single loop, either manually selecting multiple centers (using H108A-PHM as an example), or "raster-collect", a more automated approach for a larger number of crystals (using CDP-Chase as an example). | ||
- | + | Getting the Most Out of Your Crystals: Data Collection at the New High-Flux, Microfocus MX Beamlines at NSLS-II.,Miller MS, Maheshwari S, Shi W, Gao Y, Chu N, Soares AS, Cole PA, Amzel LM, Fuchs MR, Jakoncic J, Gabelli SB Molecules. 2019 Jan 30;24(3). pii: molecules24030496. doi:, 10.3390/molecules24030496. PMID:30704096<ref>PMID:30704096</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6nch" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Bacillus cereus ATCC 14579]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Gabelli SB]] | ||
+ | [[Category: Miller MS]] | ||
+ | [[Category: Shi W]] |
Current revision
Crystal structure of CDP-Chase: Raster data collection
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